蛋白激酶CK2在体内使Fas相关因子FAF1磷酸化，并影响其向细胞核的转运。
Protein kinase CK2 phosphorylates the Fas-associated factor FAF1 in vivo and influences its transport into the nucleus.
作者信息
Olsen Birgitte B, Jessen Vibeke, Højrup Peter, Issinger Olaf-Georg, Boldyreff Brigitte
机构信息
Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark.
出版信息
FEBS Lett. 2003 Jul 10;546(2-3):218-22. doi: 10.1016/s0014-5793(03)00575-1.
We previously identified the Fas-associated factor FAF1 as an in vitro substrate of protein kinase CK2 and determined Ser289 and Ser291 as phosphorylation sites. Here we demonstrate that these two serine residues are the only sites phosphorylated by CK2 in vitro, and that at least one site is phosphorylated in vivo. Furthermore, we analyzed putative physiological functions of FAF1 phosphorylation. The ability of FAF1 to potentiate Fas-induced apoptosis is not influenced by the FAF1 phosphorylation status; however, the nuclear import of a phosphorylation-deficient FAF1 mutant was delayed in comparison to wild-type FAF1.
我们之前鉴定出Fas相关因子FAF1是蛋白激酶CK2的体外底物，并确定丝氨酸289和丝氨酸291为磷酸化位点。在此我们证明，这两个丝氨酸残基是CK2在体外磷酸化的唯一位点，且在体内至少有一个位点被磷酸化。此外，我们分析了FAF1磷酸化的假定生理功能。FAF1增强Fas诱导的细胞凋亡的能力不受FAF1磷酸化状态的影响；然而，与野生型FAF1相比，磷酸化缺陷型FAF1突变体的核输入延迟。
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